# SYNTHESIS OF CARTILAGE PROTEOGLYCAN AND LINK PROTEIN

> **NIH NIH R01** · RUSH UNIVERSITY MEDICAL CENTER · 1988 · $126,977

## Abstract

Proteoglycan aggregates of cartilage play critical roles within the tissue
providing the mechanical resiliency vital for proper cartilage function.
Degenerative diseases such as osteoarthritis lead to a loss of resiliency
and damage to the cartilage itself commonly progressing to a loss of
function of the afflicted joint.  Successful nonsurgical intervention must
provide for the appropriate biological repair which includes not only
synthesis of the appropriate proteoglycan but also its appropriate
incorporation into a highly organized matrix.  Very little is known about
these processes at present.  This proposal is aimed at learning more about
mechanisms utilized by chondrocytes for the synthesis and subsequent
extracellular organization of proteoglycans.  A newly synthesized core
protein precursor is extensively modified largely through the addition of
sugars, resulting in a molecule more than 10 times its original mass.
During this synthetic process, a portion of the molecule must take on an
appropriate conformation ultimately permitting many proteoglycan molecules,
each with an associated link protein, to bind to single strands of
hyaluronic acid forming aggregates.  This proposal is directed at examining
the process at several levels includng:  1) a determination of the sequence
of events associated with the assembly of proteoglycan and link protein
into aggregates, 2) a determination of the intracellular transit time for
core protein, link protein and proteoglycan.  3) a characterization of a
newly discovered pool of intracellular core protein which may not be
converted into proteoglycan.  4) an examination of the possibility that
processing of the core protein precursor into proteoglycan includes peptide
cleavage, 5) an examination of the timing of addition of various
monosaccharides to the core protein precursor, 6) a study of the
contribution of snythesis to the heterogeneity of link protein in bovine
cartilage and a comparsion of the biosynthetic process in bovine and rat
cultures to determine what features might be common to both, 7) an
examination on the effect of oxygen or pH on cartilage cultures with
respect to the ability of newly synthesized proteoglycan to interact with
hyaluronic acid.  8) examination of the location and timing of formation of
disulfide bridges in the hyaluronic acid binding region of the proteoglycan.

## Key facts

- **NIH application ID:** 3156136
- **Project number:** 5R01AR031896-06
- **Recipient organization:** RUSH UNIVERSITY MEDICAL CENTER
- **SAM.gov UEI:** C155UU2TXCP3
- **Principal Investigator:** JAMES H KIMURA
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1988
- **Award amount:** $126,977
- **Award type:** 5
- **Project period:** 1983-07-01 → 1991-06-30

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3156136

## Citation

> US National Institutes of Health, RePORTER application 3156136, SYNTHESIS OF CARTILAGE PROTEOGLYCAN AND LINK PROTEIN (5R01AR031896-06). Retrieved via MORVS 2026-10-24 from https://api.morvs.ai/grant/nih/3156136. Licensed CC0.

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